Many thanks to good people who have responded
to my message! Apparently I have to apologize for not formulating
my question clearly enough. Here is more explanation.
According to Ewald construction, diffraction images
collected by oscillation method correspond to thin 'curved' slices of the
reciprocal space. What I am looking for is a program to generate the
reciprocal
space (as a 3D map) from these 'slices' directly, *without* any indexing or
integration of I's. This is a simple purely geometrical calculation.
This is *not* anything routinely done for normal high-quality crystal data.
For a good dataset, such a conversion should simply yield a lattice
with distinct points. For our partially-ordered crystals, this should
help us
visualizing the actual 'shapes' of our reflections (many of them
are smeared/overlapping).
My guess that folks working with semi-ordered systems, such as liquid
crystals
or lipid bilayers, should have some programs like that...
any ideas?
Thank you again,
Sergei.
Dear All,
we are dealing with a difficult case of a 'partially ordered' protein
crystal.
Here it would be very useful to view the reciprocal space
as a 3D map. Is anyone aware of a program that would convert
standard oscillation data (one-degree frames, mar225)
into such a map? What we need is a direct conversion.
There is a program in CCP4 that is able to 'visualize' the reciprocal
space, but it requires hkl's as input.
Thank you,
Sergei Strelkov
--
Prof. Sergei V. Strelkov
Laboratory for Biocrystallography
Department of Pharmaceutical Sciences, Catholic University of Leuven
Campus Gasthuisberg, O&N2 Herestraat 49 bus 822, 3000 Leuven, Belgium
Work phone: +32 16 33 08 45 Fax: +32 16 32 34 69
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E-mail: [EMAIL PROTECTED]
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